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Publication Abstract from PubMed

Insulin receptor (IR) signaling is critical to controlling nutrient uptake and metabolism. However, only a low-resolution (3.8 A) structure currently exists for the IR ectodomain, with some segments ill-defined or unmodeled due to disorder. Here, we revise this structure using new diffraction data to 3.3 A resolution that allow improved modeling of the N-linked glycans, the first and third fibronectin type III domains, and the insert domain. A novel haptic interactive molecular dynamics strategy was used to aid fitting to low-resolution electron density maps. The resulting model provides a foundation for investigation of structural transitions in IR upon ligand binding.

Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.,Croll TI, Smith BJ, Margetts MB, Whittaker J, Weiss MA, Ward CW, Lawrence MC Structure. 2016 Jan 27. pii: S0969-2126(16)00007-1. doi:, 10.1016/j.str.2015.12.014. PMID:26853939^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.